Pseudolysin
Pseudolysin | |||||||||
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Identifiers | |||||||||
EC number | 3.4.24.26 | ||||||||
CAS number | 171715-23-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Pseudolysin (EC 3.4.24.26, Pseudomonas elastase, Pseudomonas aeruginosa neutral metalloproteinase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
This enzyme belongs to the peptidase family M4 (thermolysin family).
References
- ↑ Morihara, K.; Tsuzuki, H. (1975). "Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase". Agric. Biol. Chem. 39: 1123–1128. doi:10.1271/bbb1961.39.1123.
- ↑ Nishino, N.; Powers, J.C. (1980). "Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand". J. Biol. Chem. 255: 3482–3486. PMID 6767718.
- ↑ Dreyfus, L.A.; Iglewski, B.H. (1986). "Purification and characterization of an extracellular protease of Legionella pneumophila". Infect. Immun. 70: 736–743. PMID 3512431.
- ↑ Bever, R.A.; Iglewski, B.H. (1988). "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene". J. Bacteriol. 170: 4309–4314. PMID 2842313.
- ↑ Black, W.J.; Quinn, F.D.; Tompkins, L.S. (1990). "Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase". J. Bacteriol. 172: 2608–2613. PMID 2110146.
External links
- Pseudolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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